Document Detail

Protein kinase-dependent overexpression of the nuclear protein pirin in c-JUN and RAS transformed fibroblasts.
MedLine Citation:
PMID:  10228560     Owner:  NLM     Status:  MEDLINE    
Signalling via the protein kinase Raf-MEK-ERK pathway is of major importance for transformation by oncogenes. To identify genes affected by inhibition of this pathway, c-JUN transformed rat fibroblasts were treated with a MEK1 inhibitor (PD98059) and subjected to two-dimensional gel electrophoresis after cell lysis. Gene products with expression influenced by MEK1 inhibition were determined by mass spectrometry of fragments from in-gel tryptic digestions. The expression of pirin, a nuclear factor I-interacting protein, was lowered after inhibition of MEK1. Western blot analysis revealed increased expression of pirin in RAS and c-JUN transformed cells in the absence of PD98059. Inhibition of MEK1 also led to reduced expression of alpha-enolase, phosphoglycerate kinase, elongation factor 2 and heterogeneous nuclear ribonucleoprotein A3, the latter two being detected as truncated proteins. In contrast, the level of ornithine aminotransferase was increased. We conclude that inhibition of MEK1 results in major alterations of protein expression in c-JUN transformed cells, suggesting that this pathway is important for oncogene-induced phenotypic changes.
A C Bergman; A A Alaiya; W Wendler; B Binetruy; M Shoshan; K Sakaguchi; T Bergman; U Kronenwett; G Auer; E Appella; H Jörnvall; S Linder
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cellular and molecular life sciences : CMLS     Volume:  55     ISSN:  1420-682X     ISO Abbreviation:  Cell. Mol. Life Sci.     Publication Date:  1999 Mar 
Date Detail:
Created Date:  1999-05-19     Completed Date:  1999-05-19     Revised Date:  2013-06-03    
Medline Journal Info:
Nlm Unique ID:  9705402     Medline TA:  Cell Mol Life Sci     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  467-71     Citation Subset:  IM    
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
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MeSH Terms
Calcium-Calmodulin-Dependent Protein Kinases / physiology
Carrier Proteins / biosynthesis*,  genetics
Cell Line, Transformed
Cell Transformation, Neoplastic / genetics*
Fibroblasts / drug effects,  metabolism*
Flavonoids / pharmacology
Genes, jun*
Genes, ras*
Heterogeneous-Nuclear Ribonucleoproteins
MAP Kinase Kinase 1
Mass Spectrometry
Mitogen-Activated Protein Kinase 1
Mitogen-Activated Protein Kinase 3
Mitogen-Activated Protein Kinase Kinases*
Mitogen-Activated Protein Kinases*
Nuclear Proteins / biosynthesis*,  genetics
Ornithine-Oxo-Acid Transaminase / biosynthesis,  genetics
Peptide Elongation Factor 2
Peptide Elongation Factors / biosynthesis,  genetics
Phosphoglycerate Kinase / biosynthesis,  genetics
Phosphopyruvate Hydratase / biosynthesis,  genetics
Protein-Serine-Threonine Kinases / antagonists & inhibitors,  physiology*
Protein-Tyrosine Kinases / antagonists & inhibitors,  physiology*
Proto-Oncogene Proteins c-raf / physiology
Ribonucleoproteins / biosynthesis,  genetics
Signal Transduction / genetics*
Reg. No./Substance:
0/2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one; 0/Carrier Proteins; 0/Flavonoids; 0/Heterogeneous-Nuclear Ribonucleoproteins; 0/Nuclear Proteins; 0/PIR protein, human; 0/Peptide Elongation Factor 2; 0/Peptide Elongation Factors; 0/Ribonucleoproteins; EC Transaminase; EC 2.7.1.-/MAP2K1 protein, human; EC Kinases; EC Kinases; EC Proteins c-raf; EC Protein Kinases; EC Protein Kinase 1; EC Protein Kinase 3; EC Protein Kinases; EC Kinase Kinase 1; EC Protein Kinase Kinases; EC Kinase; EC Hydratase

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